ID A0A340X4D4_LIPVE Unreviewed; 1128 AA.
AC A0A340X4D4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Cytosolic carboxypeptidase 1 {ECO:0000256|ARBA:ARBA00041044};
DE EC=3.4.17.24 {ECO:0000256|ARBA:ARBA00026108};
DE AltName: Full=ATP/GTP-binding protein 1 {ECO:0000256|ARBA:ARBA00043070};
DE AltName: Full=Protein deglutamylase CCP1 {ECO:0000256|ARBA:ARBA00043068};
GN Name=AGTPBP1 {ECO:0000313|RefSeq:XP_007456176.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007456176.1};
RN [1] {ECO:0000313|RefSeq:XP_007456176.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O
CC = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-
CC glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-
CC COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623;
CC Evidence={ECO:0000256|ARBA:ARBA00029302};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005;
CC Evidence={ECO:0000256|ARBA:ARBA00029302};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] +
CC H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-
CC glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-
CC COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555,
CC ChEBI:CHEBI:149556; EC=3.4.17.24;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793;
CC Evidence={ECO:0000256|ARBA:ARBA00024524};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR RefSeq; XP_007456176.1; XM_007456114.1.
DR AlphaFoldDB; A0A340X4D4; -.
DR GeneID; 103082044; -.
DR CTD; 23287; -.
DR OrthoDB; 168164at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06906; M14_Nna1; 1.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033852; CBPC1/4.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR12756; CYTOSOLIC CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR12756:SF24; CYTOSOLIC CARBOXYPEPTIDASE 1; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|RefSeq:XP_007456176.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|RefSeq:XP_007456176.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000313|RefSeq:XP_007456176.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300}.
FT DOMAIN 614..704
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 780..886
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 126707 MW; 92BF728F296DDF6E CRC64;
MTAKGSTGME VLLSTLENTK DLQTTLNILS ILVELVSAGG GRRASFLVSK GGSQILLQLL
MNASKESPLN EELMVQIHSI LAKIGPKDKK FGAKARINGA LNITLNLVKQ NLQNHRLVLP
CLQLLRVYSA NSVNSVSLGK NGVVELMFKI IGPFSKKNSS LMKVALDTLA ALLKSKTNAR
RAVDRGYVQV LLTIYVDWHR HDNRHRNMLI RKGILQSLKS VTSIKLGRKA FIDANGMKIL
YNTSQLPVIP VTGPVAQLYS LPPEVDDVVD ESDDNDDIDL EAENETENED DLDKNFKNDD
IETDINKLKP QQEPGRTIEE LKMYEHLFPE LVDDFQDYDL ISREPKAFVF EGKVRGPIVV
PTAGEEASGN SSNLRKGVVM KATVSPKGDE DNKKPACADL AKEDIKDNDR TLQQQLGDQN
RTISSGHGLN NDIVKALDRI TLRNIPSRTA PGFTAGMKGY SLPVTALTCA NACSHVATCG
NVLFEGRTVQ LGKLCCTGVE TEDDEDTEST ASAEQALVEV PGGPTLHDSD LYIEIVKSTK
SVPEYSEVAY PDYFGHIPPP FKEPILERPY GVQRTKIAQD IERLIHQSDI IDRVVYDLDN
PNYSTPEEGD ILKFNSKFES GNLRKVIQIR KNEYDLILNS DINSNHYHQW FYFEVSGMRP
SIAYRFNIIN CEKSNSQFNY GMQPLMYSVQ EALNARPWWI RVGTDICYYK NHFSRSSIAA
GGQKGKSYYT ITFTVIFPHK DDVCYFAYHY PYTYSTLQMH LQKLESAHNP QQIYFRKDVL
CETLSGNSCP LVTITAMPES NYYEHICQFR NRPYVFLSAR VHPGETNASW VMKGTLEYLM
SNNPTAQSLR ESYIFKIVPM LNPDGVINGN HRCSLSGEDL NRQWQSPNPD LHPTIYHAKG
LLQYLAAVKH LPLVYCDYHG HSRKKNVFMY GCSIKETVWH TNDNAASCDV VEDVGYRTLP
KILSHIAPAF CMSSCSFVVE KSKESTARVV VWREIGVQRS YTMESTLCGC DQGKYKGLQI
GTRELEEMGA KFCVGLLRLK RLTSPLEYNL PSSLLDFEND LIESSCKVTS PTTYVLDEDE
PRFLEEVDYS AESNDELDIE LAENAGDYEP SAQEDVLSDS ELSRTYLP
//
